ABCC7 p.Ser1118Gln
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PMID: 23955087
[PubMed]
Wang W et al: "Relative contribution of different transmembrane segments to the CFTR chloride channel pore."
No.
Sentence
Comment
153
In contrast, S1118A had no effect on conductance, while S1118Q and S1118V were associated with Fig. 7 Thiocyanate permeability of mutants.
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ABCC7 p.Ser1118Gln 23955087:153:56
status: NEW183 Acetate permeability was slightly increased in S1118A and T1115A, but not significantly changed in S1118Q or S1118V (Fig. 8b).
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ABCC7 p.Ser1118Gln 23955087:183:99
status: NEW208 Neither S1118A nor T1115A significantly altered single channel conductance, although introduction of larger amino acid side chains in S1118Q and S1118V led to very small decreases in conductance (Fig. 5).
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ABCC7 p.Ser1118Gln 23955087:208:134
status: NEW211 Reduction of side chain volume in S1118A and T1115A, like T338A, led to an increase in the relative permeability of the small organic anion acetate, consistent with an increase in the apparent diameter of the narrowest region of the pore [25, 26]; however, introduction of side chains with larger volume (S1118Q, S1118V) did not lead to a decrease in acetate permeability (Fig. 8).
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ABCC7 p.Ser1118Gln 23955087:211:305
status: NEW219 Previously, the S1118C mutation was shown to decrease conductance at positive voltages, leading to inward rectification of both the single channel and macroscopic current-voltage relationships [10], and although this would be considered a very conservative mutation (one oxygen atom replaced by sulfur) this effect was not reproduced in S1118A, S1118Q or S1118 (Fig. 5).
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ABCC7 p.Ser1118Gln 23955087:219:345
status: NEW